We are actively tracking the number of publications by the scientific community which reference our structures, whether in the main text, figure captions or supplementary material. Selected articles are manually reviewed. Publications by SSGCID authors are excluded from the manually reviewed list. From our manual curation results, we estimate that the false positive rate might be as high as 50% for some structures.
This list was obtained from Google Scholar searches using an API provided by Christian Kreibich.
| Structure | Year released | #citations |
|---|---|---|
| 6V91 | 2020 | 0 |
| 4XKZ | 2015 | 0 |
| 6VH5 | 2020 | 0 |
| 4W9U | 2014 | 0 |
| 6VS4 | 2020 | 0 |
| 5TT1 | 2016 | 0 |
| 5VC2 | 2017 | 0 |
| 4XGH | 2015 | 0 |
| 6W14 | 2020 | 0 |
| 6W15 | 2020 | 0 |
| # | PDB | Additional SSGCID structures cited | Link | Title | Year | Citation | Highlighted abstract |
|---|---|---|---|---|---|---|---|
| 1 | 3o0h | - | https://www.degruyter.com/view/j/zkri.ahead-of-print/zkri-2018-2064/zkri-2018-20... | Sulfur (lone-pair) interactions with FAD in flavoenzymes | 2018 | RFN Silva, ACS Sacco, I Caracelli- Zeitschrift fr, 2018 - degruyter.com | The interactions of π-systems with lone-pairs of electrons are known and have been described in biological systems, involving lone-pairs derived from metals, metalloids, sulphur, oxygen and nitrogen. This study describes a bibliographic survey of the disulphide-bound sulphur(lone-pair) interactions with -systems residing in the flavin ad Also, the S(lp)…π(FAD) interaction in the 1K4Q [64] and 3O0H [65] proteins show the orientation of sulphur-lp to the Ct(U) centroid, F |
| 2 | 3o0h | - | http://eprints.sunway.edu.my/893/ | Sulphur (lone pair) interactions with FAD in flavoenzymes | 2018 | RFN Silva, ACS Sacco, I Caracelli- Zeitschrift fur, 2018 - eprints.sunway.edu.my | Finally, in the 22 SOX enzymes found in PDB , there were 45 monomers having FAD S(lp)(FAD) interactions in three examples of GR enzymes: (a) 1K4Q [64], (b) 3O0H [64] and with FAD via S(lp)(FAD) interactions that pro- vide stability to the secondary structure and |
| 3 | 3nwo | - | https://link.springer.com/article/10.1007/s11010-021-04121-5 | The rise and fall of anandamide: processes that control synthesis, degradation, and storage | 2021 | RG Biringer- Molecular and Cellular Biochemistry, 2021 - Springer | This manuscript discusses the key enzymes in AEA homeostasis, in terms of structure , reaction specificity, enzymatic activity, regulation, and tissue and cellular expression patterns with a focus on the human isoforms involved. ... No X-ray structures or posttranslational modifications have been reported. There are two potential structural model templates suggested on the SWISS-MODEL website [14], template 3nwo.1.A and template 5mxp.1.B. hABHD4 is produced |
| 4 | 4gri | - | https://journals.asm.org/doi/abs/10.1128/ecosalplus.ESP-0002-2016 | Aminoacyl-tRNA synthetases in the bacterial world | 2016 | R Gieg, M Springer- EcoSal Plus, 2016 - Am Soc Microbiol | Note that aaRSs requiring cognate tRNA for activation can tightly bind their amino acid substrates in the absence of tRNA, thereby leading to inactive conformers as seen, e.g., in E. coli ArgRS (4oby) (178) and B. burgdorferi GluRS (4gri) (unpublished from the Seattle Structure Genomics Center for Infectious Disease). |
| 5 | 5t8s | - | https://www.biorxiv.org/content/10.1101/622068v2.full.pdf | MCSS-based Predictions of Binding Mode and Selectivity of Nucleotide Ligands | 2020 | R Gonzalez-Aleman, N Chevrollier, M Simoes- bioRxiv, 2020 - biorxiv.org | method based on a coarse-grained model (RNA-LIM) was developed to model the structure of an on the protein-nucleotide complexes currently available in the Protein Data Bank (RCSB PDB (52 less than 2.0 and thus not representative of the currently available structural data |
| 6 | 6wps | 6vxx | https://academic.oup.com/nar/article-abstract/49/D1/D282/5901966 | CoV3D: a database of high resolution coronavirus protein structures | 2021 | R Gowthaman, JD Guest, R Yin- Nucleic acids, 2021 - academic.oup.com | (A) Visualization of the superposed spike RBD complexes with antibody S309 ( PDB code 6WPS ) ( 20 ) and (B) A trimeric spike structure in RBD-closed conformation ( 5 ) ( PDB code 6VXX Park YJ, Tortorici MA, Wall A., McGuire AT and Veesler D. (2020) Structure , Function, and |
| 7 | 3u0d | - | http://www.jbc.org/content/294/51/19523.short | The structure of the bacterial ironcatecholate transporter Fiu suggests that it imports substrates via a two-step mechanism | 2019 | R Grinter, T Lithgow- Journal of Biological Chemistry, 2019 - ASBMB | TBDTs are highly divergent in sequence but share a common structural architecture , consisting of a 22 The structure of Fiu consists of a 22-stranded transmembrane -barrel characteristic of the DALI web server (37) identified PiuA from Acinetobacter baumannii ( PDB code 5FP1 |
| 8 | 6nb6 | - | https://www.sciencedirect.com/science/article/pii/S0021925817484729 | SARS-CoV-2 (COVID-19) structural and evolutionary dynamicome: Insights into functional evolution and human genomics | 2020 | R Gupta, J Charron, CL Stenger, J Painter- Journal of Biological, 2020 - Elsevier | receptor structure -function. post-translational modification (PTM). COVID-19. severe acute respiratory coronavirus 2 (SARS-CoV-2) Their 2633-kb genome consists of positive-sense, single-stranded RNA, coding for nonstructural and structural proteins This protein complex model was built through the integration of PDB structures 6CRW, 6NB6, and 5X58 for the trimer of spike proteins with 6M17, |
| 9 | 6vxx | 6vyb | https://www.ncbi.nlm.nih.gov/pmc/articles/pmc7337389/ | Glycans on the SARS-CoV-2 spike control the receptor binding domain conformation | 2020 | R Henderson, RJ Edwards, K Mansouri, K Janowska- bioRxiv, 2020 - ncbi.nlm.nih.gov | this map yielding a structure aligning to the unmutated 2P structure ( PDB ID 6VXX ) with a one RBD 'up' state structure fit to this map to its unmutated counterpart ( PDB ID 6VYB N234A mutation (Figure 3E and andF).F). However, the limited resolution of this structure limits close |
| 10 | 6q04 | - | https://www.nature.com/articles/s41594-020-0479-4 | Controlling the SARS-CoV-2 spike glycoprotein conformation | 2020 | R Henderson, RJ Edwards, K Mansouri- Nature structural &, 2020 - nature.com | d, The SARS-2 (left, PDB 6VXX) and MERS (right, PDB 6Q04 ) structures , each with a single protomer depicted in cartoon of the gj angles and dihedrals overlaid on an alignment between a SARS-2 down (cartoon structure with black centroids and lines; PDB 6VXX) and |